IDH2

Functionⁱ

Plays a role in intermediary metabolism and energy production. It may tightly associate or interact with the pyruvate dehydrogenase complex.

Catalytic activityⁱ

Isocitrate + NADP⁺ = 2-oxoglutarate + CO₂ + NADPH.

Cofactorⁱ

Mg²⁺By similarity, Mn²⁺By similarityNote: Binds 1 Mg²⁺ or Mn²⁺ ion per subunit.By similarity

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	117	SubstrateBy similarity	1
Binding siteⁱ	122	NADPBy similarity	1
Binding siteⁱ	149	SubstrateBy similarity	1
Binding siteⁱ	172	SubstrateBy similarity	1
Siteⁱ	179	Critical for catalysisBy similarity	1
Siteⁱ	251	Critical for catalysisBy similarity	1
Metal bindingⁱ	291	Magnesium or manganeseBy similarity	1
Binding siteⁱ	299	NADPBy similarity	1
Metal bindingⁱ	314	Magnesium or manganeseBy similarity	1
Binding siteⁱ	367	NADP; via amide nitrogen and carbonyl oxygenBy similarity	1

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Nucleotide bindingⁱ	115 – 117	NADPBy similarity		3
Nucleotide bindingⁱ	349 – 354	NADPBy similarity		6

GO - Molecular functionⁱ

isocitrate dehydrogenase (NADP+) activity
Source: CACAO
Inferred from direct assayⁱ
- 23226729
magnesium ion binding Source: UniProtKB
NAD binding Source: InterPro
protein homodimerization activity
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

2-oxoglutarate metabolic process Source: UniProtKB
carbohydrate metabolic process
Source: ProtInc
Non-traceable author statementⁱ
- 8954790
glyoxylate cycle Source: UniProtKB-KW
isocitrate metabolic process Source: UniProtKB
NADP biosynthetic process Source: Ensembl
NADP metabolic process
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
negative regulation of glial cell migration Source: Ensembl
negative regulation of glial cell proliferation Source: Ensembl
negative regulation of matrix metallopeptidase secretion Source: Ensembl
tricarboxylic acid cycle Source: Reactome

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Oxidoreductase
Biological process	Glyoxylate bypass, Tricarboxylic acid cycle
Ligand	Magnesium, Manganese, Metal-binding, NADP

Enzyme and pathway databases

BioCycⁱ	MetaCyc:HS00021-MONOMER
BRENDAⁱ	1.1.1.42 2681
Reactomeⁱ	R-HSA-2151201 Transcriptional activation of mitochondrial biogenesis R-HSA-71403 Citric acid cycle (TCA cycle)
SIGNORⁱ	P48735

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Isocitrate dehydrogenase [NADP], mitochondrial (EC:1.1.1.42) Short name: IDH Alternative name(s): ICD-M IDP NADP(+)-specific ICDH Oxalosuccinate decarboxylase
Gene namesⁱ	Name:IDH2
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 15

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000182054.9
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:5383 IDH2
MIMⁱ	147650 gene
neXtProtⁱ	NX_P48735

Keywords - Cellular componentⁱ

Mitochondrion

Pathology & Biotechⁱ

Involvement in diseaseⁱ

D-2-hydroxyglutaric aciduria 2 (D2HGA2)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA neurometabolic disorder causing developmental delay, epilepsy, hypotonia, and dysmorphic features. Both a mild and a severe phenotype exist. The severe phenotype is homogeneous and is characterized by early infantile-onset epileptic encephalopathy and cardiomyopathy. The mild phenotype has a more variable clinical presentation. Diagnosis is based on the presence of an excess of D-2-hydroxyglutaric acid in the urine.

Glioma (GLM)2 Publications

The gene represented in this entry is involved in disease pathogenesis.

Disease descriptionGliomas are benign or malignant central nervous system neoplasms derived from glial cells. They comprise astrocytomas and glioblastoma multiforme that are derived from astrocytes, oligodendrogliomas derived from oligodendrocytes and ependymomas derived from ependymocytes.

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_073181	158	P → L in GLM; somatic mutation. 1 Publication	1
Natural variantⁱVAR_073182	162	P → S in GLM; somatic mutation. 1 Publication	1
Natural variantⁱVAR_073183	172	R → G in GLM; somatic mutation; reduces enzymatic activity. 1 PublicationCorresponds to variant dbSNP:rs1057519906Ensembl.	1
Natural variantⁱVAR_073184	172	R → K in GLM; somatic mutation; reduces enzymatic activity. 2 PublicationsCorresponds to variant dbSNP:rs121913503Ensembl.	1
Natural variantⁱVAR_073185	172	R → M in GLM; somatic mutation; reduces enzymatic activity. 1 Publication	1

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	413	K → A: 44-fold loss in activity. 1 Publication	1
Mutagenesisⁱ	413	K → Q: 20-fold decrease in Vmax. 1 Publication	1
Mutagenesisⁱ	413	K → R: No appreciable difference in Km for isocitrate and NADP. 1 Publication	1

Keywords - Diseaseⁱ

Disease mutation

Organism-specific databases

DisGeNET More...DisGeNETⁱ	3418
MalaCards human disease database More...MalaCardsⁱ	IDH2
MIMⁱ	137800 phenotype 613657 phenotype
Open Targets More...OpenTargetsⁱ	ENSG00000182054
Orphanetⁱ	251589 Anaplastic astrocytoma 251663 Anaplastic oligoastrocytoma 251630 Anaplastic oligodendroglioma 79315 D-2-hydroxyglutaric aciduria 296 Enchondromatosis 251601 Fibrillary astrocytoma 251604 Gemistocytic astrocytoma 163634 Maffucci syndrome 251656 Oligoastrocytoma 251627 Oligodendroglioma 251598 Protoplasmic astrocytoma
PharmGKBⁱ	PA29631

Chemistry databases

ChEMBLⁱ	CHEMBL3991501
Drug and drug target database More...DrugBankⁱ	DB01727 Isocitric Acid

Polymorphism and mutation databases

BioMutaⁱ	IDH2
DMDMⁱ	20141568

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Transit peptideⁱ	1 – 39	MitochondrionBy similarityAdd BLAST		39
ChainⁱPRO_0000014420	40 – 452	Isocitrate dehydrogenase [NADP], mitochondrialAdd BLAST		413

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	45	N6-acetyllysineBy similarity	1
Modified residueⁱ	48	N6-acetyllysineBy similarity	1
Modified residueⁱ	67	N6-acetyllysineCombined sources	1
Modified residueⁱ	69	N6-acetyllysineBy similarity	1
Modified residueⁱ	80	N6-acetyllysine; alternateBy similarity	1
Modified residueⁱ	80	N6-succinyllysine; alternateBy similarity	1
Modified residueⁱ	106	N6-acetyllysine; alternateCombined sources	1
Modified residueⁱ	106	N6-succinyllysine; alternateBy similarity	1
Modified residueⁱ	155	N6-acetyllysineCombined sources	1
Modified residueⁱ	166	N6-acetyllysine; alternateCombined sources	1
Modified residueⁱ	166	N6-succinyllysine; alternateBy similarity	1
Modified residueⁱ	180	N6-acetyllysine; alternateCombined sources	1
Modified residueⁱ	180	N6-succinyllysine; alternateBy similarity	1
Modified residueⁱ	193	N6-acetyllysine; alternateBy similarity	1
Modified residueⁱ	193	N6-succinyllysine; alternateBy similarity	1
Modified residueⁱ	199	N6-acetyllysineBy similarity	1
Modified residueⁱ	256	N6-acetyllysine; alternateCombined sources	1
Modified residueⁱ	256	N6-succinyllysine; alternateBy similarity	1
Modified residueⁱ	263	N6-acetyllysineCombined sources	1
Modified residueⁱ	272	N6-acetyllysineCombined sources	1
Modified residueⁱ	275	N6-acetyllysineCombined sources	1
Modified residueⁱ	280	N6-acetyllysineBy similarity	1
Modified residueⁱ	282	N6-acetyllysine; alternateCombined sources	1
Modified residueⁱ	282	N6-succinyllysine; alternateBy similarity	1
Modified residueⁱ	384	N6-acetyllysine; alternateBy similarity	1
Modified residueⁱ	384	N6-succinyllysine; alternateBy similarity	1
Modified residueⁱ	400	N6-acetyllysineBy similarity	1
Modified residueⁱ	413	N6-acetyllysine1 Publication	1
Modified residueⁱ	442	N6-acetyllysineCombined sources	1

Post-translational modificationⁱ

Acetylation at Lys-413 dramatically reduces catalytic activity. Deacetylated by SIRT3.1 Publication

Keywords - PTMⁱ

Acetylation

Proteomic databases

EPDⁱ	P48735
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P48735
PaxDbⁱ	P48735
PeptideAtlas More...PeptideAtlasⁱ	P48735
PRIDEⁱ	P48735
ProteomicsDBⁱ	55932

2D gel databases

USC-OGP 2-DE database More...OGPⁱ	P48735
UCD-2DPAGEⁱ	P48735

PTM databases

CarbonylDBⁱ	P48735
iPTMnetⁱ	P48735
PhosphoSitePlusⁱ	P48735
SwissPalmⁱ	P48735

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSG00000182054 Expressed in 236 organ(s), highest expression level in muscle of leg
CleanExⁱ	HS_IDH2
ExpressionAtlasⁱ	P48735 baseline and differential
Genevisibleⁱ	P48735 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	HPA007831

HPAⁱ

HPA007831

Interactionⁱ

Subunit structureⁱ

Homodimer.

GO - Molecular functionⁱ

protein homodimerization activity
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	109644, 37 interactors
Database of interacting proteins More...DIPⁱ	DIP-61416N
IntActⁱ	P48735, 11 interactors
Molecular INTeraction database More...MINTⁱ	P48735
STRINGⁱ	9606.ENSP00000331897

Chemistry databases

BindingDBⁱ

P48735

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	50 – 54	Combined sources	5
Helixⁱ	57 – 69	Combined sources	13
Turnⁱ	70 – 74	Combined sources	5
Beta strandⁱ	79 – 83	Combined sources	5
Helixⁱ	86 – 91	Combined sources	6
Turnⁱ	92 – 94	Combined sources	3
Helixⁱ	95 – 107	Combined sources	13
Beta strandⁱ	108 – 112	Combined sources	5
Helixⁱ	120 – 126	Combined sources	7
Helixⁱ	135 – 143	Combined sources	9
Beta strandⁱ	146 – 151	Combined sources	6
Beta strandⁱ	169 – 173	Combined sources	5
Helixⁱ	177 – 180	Combined sources	4
Beta strandⁱ	182 – 186	Combined sources	5
Beta strandⁱ	190 – 196	Combined sources	7
Beta strandⁱ	205 – 214	Combined sources	10
Beta strandⁱ	216 – 220	Combined sources	5
Helixⁱ	225 – 242	Combined sources	18
Beta strandⁱ	246 – 250	Combined sources	5
Turnⁱ	252 – 254	Combined sources	3
Helixⁱ	258 – 273	Combined sources	16
Helixⁱ	275 – 280	Combined sources	6
Beta strandⁱ	285 – 289	Combined sources	5
Helixⁱ	290 – 299	Combined sources	10
Beta strandⁱ	304 – 308	Combined sources	5
Helixⁱ	310 – 324	Combined sources	15
Beta strandⁱ	329 – 335	Combined sources	7
Beta strandⁱ	342 – 345	Combined sources	4
Helixⁱ	352 – 359	Combined sources	8
Helixⁱ	369 – 386	Combined sources	18
Helixⁱ	389 – 407	Combined sources	19
Helixⁱ	413 – 420	Combined sources	8
Helixⁱ	422 – 424	Combined sources	3
Turnⁱ	427 – 429	Combined sources	3
Helixⁱ	434 – 449	Combined sources	16

Show more details

3D structure databases

ProteinModelPortalⁱ	P48735
SMRⁱ	P48735
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	134 – 140	Substrate bindingBy similarity		7

Sequence similaritiesⁱ

Belongs to the isocitrate and isopropylmalate dehydrogenases family.Curated

Keywords - Domainⁱ

Transit peptide

Phylogenomic databases

eggNOGⁱ	KOG1526 Eukaryota COG0538 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00390000012547
HOGENOMⁱ	HOG000019858
HOVERGENⁱ	HBG006119
InParanoidⁱ	P48735
KEGG Orthology (KO) More...KOⁱ	K00031
OMAⁱ	FEKHYKP
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G06IY
PhylomeDBⁱ	P48735
TreeFamⁱ	TF300428

Family and domain databases

InterProⁱ	View protein in InterPro IPR019818 IsoCit/isopropylmalate_DH_CS IPR004790 Isocitrate_DH_NADP IPR024084 IsoPropMal-DH-like_dom
PANTHERⁱ	PTHR11822 PTHR11822, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00180 Iso_dh, 1 hit
PIRSFⁱ	PIRSF000108 IDH_NADP, 1 hit
SMARTⁱ	View protein in SMART SM01329 Iso_dh, 1 hit
TIGRFAMsⁱ	TIGR00127 nadp_idh_euk, 1 hit
PROSITEⁱ	View protein in PROSITE PS00470 IDH_IMDH, 1 hit

Sequences (2+)ⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 2 described isoforms and 2 potential isoforms that are computationally mapped.Show all Align All

Isoform 1 (identifier: P48735-1) [UniParc]FASTA Add to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAGYLRVVRS LCRASGSRPA WAPAALTAPT SQEQPRRHYA DKRIKVAKPV 
        60         70         80         90        100
VEMDGDEMTR IIWQFIKEKL ILPHVDIQLK YFDLGLPNRD QTDDQVTIDS 
       110        120        130        140        150
ALATQKYSVA VKCATITPDE ARVEEFKLKK MWKSPNGTIR NILGGTVFRE 
       160        170        180        190        200
PIICKNIPRL VPGWTKPITI GRHAHGDQYK ATDFVADRAG TFKMVFTPKD 
       210        220        230        240        250
GSGVKEWEVY NFPAGGVGMG MYNTDESISG FAHSCFQYAI QKKWPLYMST 
       260        270        280        290        300
KNTILKAYDG RFKDIFQEIF DKHYKTDFDK NKIWYEHRLI DDMVAQVLKS 
       310        320        330        340        350
SGGFVWACKN YDGDVQSDIL AQGFGSLGLM TSVLVCPDGK TIEAEAAHGT 
       360        370        380        390        400
VTRHYREHQK GRPTSTNPIA SIFAWTRGLE HRGKLDGNQD LIRFAQMLEK 
       410        420        430        440        450
VCVETVESGA MTKDLAGCIH GLSNVKLNEH FLNTTDFLDT IKSNLDRALG 

RQ

Length:452

Mass (Da):50,909

Last modified:April 3, 2002 - v2

Checksum:ⁱ4DDC830AFC06AB52

GO

Isoform 2 (identifier: P48735-2) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
1-52: Missing.

« Hide

        10         20         30         40         50
MDGDEMTRII WQFIKEKLIL PHVDIQLKYF DLGLPNRDQT DDQVTIDSAL 
        60         70         80         90        100
ATQKYSVAVK CATITPDEAR VEEFKLKKMW KSPNGTIRNI LGGTVFREPI 
       110        120        130        140        150
ICKNIPRLVP GWTKPITIGR HAHGDQYKAT DFVADRAGTF KMVFTPKDGS 
       160        170        180        190        200
GVKEWEVYNF PAGGVGMGMY NTDESISGFA HSCFQYAIQK KWPLYMSTKN 
       210        220        230        240        250
TILKAYDGRF KDIFQEIFDK HYKTDFDKNK IWYEHRLIDD MVAQVLKSSG 
       260        270        280        290        300
GFVWACKNYD GDVQSDILAQ GFGSLGLMTS VLVCPDGKTI EAEAAHGTVT 
       310        320        330        340        350
RHYREHQKGR PTSTNPIASI FAWTRGLEHR GKLDGNQDLI RFAQMLEKVC 
       360        370        380        390        400
VETVESGAMT KDLAGCIHGL SNVKLNEHFL NTTDFLDTIK SNLDRALGRQ

Note: No experimental confirmation available.

Show »

Length:400

Mass (Da):45,180

Checksum:ⁱF1274A2EC2243D5E

GO

Computationally mapped potential isoform sequencesⁱ

There are 2 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

H0YL11	H0YL11_HUMAN	Isocitrate dehydrogenase [NADP], mi... Isocitrate dehydrogenase [NADP], mitochondrial	IDH2	312	Annotation score:
H0YLL5	H0YLL5_HUMAN	Isocitrate dehydrogenase [NADP], mi... Isocitrate dehydrogenase [NADP], mitochondrial	IDH2	38	Annotation score:

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	34	Q → H in CAA49208 (Ref. 1) Curated		1
Sequence conflictⁱ	435	T → M in CAA49208 (Ref. 1) Curated		1

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_065174	140	R → G in D2HGA2. 1 PublicationCorresponds to variant dbSNP:rs267606870Ensembl.	1
Natural variantⁱVAR_065175	140	R → Q in D2HGA2. 1 PublicationCorresponds to variant dbSNP:rs121913502EnsemblClinVar.	1
Natural variantⁱVAR_073181	158	P → L in GLM; somatic mutation. 1 Publication	1
Natural variantⁱVAR_073182	162	P → S in GLM; somatic mutation. 1 Publication	1
Natural variantⁱVAR_073183	172	R → G in GLM; somatic mutation; reduces enzymatic activity. 1 PublicationCorresponds to variant dbSNP:rs1057519906Ensembl.	1
Natural variantⁱVAR_073184	172	R → K in GLM; somatic mutation; reduces enzymatic activity. 2 PublicationsCorresponds to variant dbSNP:rs121913503Ensembl.	1
Natural variantⁱVAR_073185	172	R → M in GLM; somatic mutation; reduces enzymatic activity. 1 Publication	1
Natural variantⁱVAR_076512	172	R → S Found in patients with cartilagenous tumors. 1 PublicationCorresponds to variant dbSNP:rs1057519736Ensembl.	1
Natural variantⁱVAR_076513	172	R → T Found in patients with cartilagenous tumors. 1 Publication	1
Natural variantⁱVAR_076514	172	R → W Found in patients with cartilagenous tumors. 1 Publication	1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_056278	1 – 52	Missing in isoform 2. 1 PublicationAdd BLAST		52

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X69433 mRNA Translation: CAA49208.1 AK294148 mRNA Translation: BAG57473.1 AK312627 mRNA Translation: BAG35513.1 AK316388 mRNA Translation: BAH14759.1 AC087284 Genomic DNA No translation available. AC092769 Genomic DNA No translation available. CH471101 Genomic DNA Translation: EAX02082.1 BC009244 mRNA Translation: AAH09244.1 BC071828 mRNA Translation: AAH71828.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS10359.1 [P48735-1] CCDS76792.1 [P48735-2]
PIRⁱ	S57499
NCBI Reference Sequences More...RefSeqⁱ	NP_001276839.1, NM_001289910.1 [P48735-2] NP_001277043.1, NM_001290114.1 NP_002159.2, NM_002168.3 [P48735-1]
UniGeneⁱ	Hs.596461

Genome annotation databases

Ensemblⁱ	ENST00000330062; ENSP00000331897; ENSG00000182054 [P48735-1] ENST00000540499; ENSP00000446147; ENSG00000182054 [P48735-2]
GeneIDⁱ	3418
KEGGⁱ	hsa:3418
UCSC genome browser More...UCSCⁱ	uc002box.4 human [P48735-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P48735	Isoform 2 of Isocitrate dehydrogenase [NADP], mitochondrial		HUMAN		400	UniRef100_P48735
cDNA FLJ50654, highly similar to Isocitrate dehydrogenase		HUMAN		322

Protein	Similar proteins		Species	Score	Length	Source
P48735	Isocitrate dehydrogenase [NADP], mitochondrial		RAT		452	UniRef90_P48735
Isocitrate dehydrogenase [NADP], mitochondrial	)	MOUSE		452
Isocitrate dehydrogenase [NADP], mitochondrial		MACFA		452
Isocitrate dehydrogenase [NADP], mitochondrial		BOVIN		452
Isoform 2 of Isocitrate dehydrogenase [NADP], mitochondrial		HUMAN		400
+117

Protein	Similar proteins		Species	Score	Length	Source
P48735	Isocitrate dehydrogenase [NADP], mitochondrial		RAT		452	UniRef50_P48735
Isocitrate dehydrogenase [NADP], mitochondrial		MACFA		452
Isocitrate dehydrogenase [NADP], mitochondrial	)	MOUSE		452
Isocitrate dehydrogenase [NADP], mitochondrial		BOVIN		452
Isoform 2 of Isocitrate dehydrogenase [NADP], mitochondrial		HUMAN		400
+209

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X69433 mRNA Translation: CAA49208.1 AK294148 mRNA Translation: BAG57473.1 AK312627 mRNA Translation: BAG35513.1 AK316388 mRNA Translation: BAH14759.1 AC087284 Genomic DNA No translation available. AC092769 Genomic DNA No translation available. CH471101 Genomic DNA Translation: EAX02082.1 BC009244 mRNA Translation: AAH09244.1 BC071828 mRNA Translation: AAH71828.1
CCDSⁱ	CCDS10359.1 [P48735-1] CCDS76792.1 [P48735-2]
PIRⁱ	S57499
RefSeqⁱ	NP_001276839.1, NM_001289910.1 [P48735-2] NP_001277043.1, NM_001290114.1 NP_002159.2, NM_002168.3 [P48735-1]
UniGeneⁱ	Hs.596461

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	4JA8	X-ray	1.55	A/B	41-452	[»]
	5GIS	X-ray	1.93	C	165-180	[»]
	5I95	X-ray	1.54	A	40-452	[»]
	5I96	X-ray	1.55	A/B	1-452	[»]
	5SVN	X-ray	2.10	A/B	40-452	[»]
	5SVO	X-ray	1.87	A/B	40-452	[»]
	6ADI	X-ray	1.97	A/B	41-452	[»]
ProteinModelPortalⁱ	P48735
SMRⁱ	P48735
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	109644, 37 interactors
DIPⁱ	DIP-61416N
IntActⁱ	P48735, 11 interactors
MINTⁱ	P48735
STRINGⁱ	9606.ENSP00000331897

Chemistry databases

BindingDBⁱ	P48735
ChEMBLⁱ	CHEMBL3991501
DrugBankⁱ	DB01727 Isocitric Acid

PTM databases

CarbonylDBⁱ	P48735
iPTMnetⁱ	P48735
PhosphoSitePlusⁱ	P48735
SwissPalmⁱ	P48735

Polymorphism and mutation databases

BioMutaⁱ	IDH2
DMDMⁱ	20141568

2D gel databases

OGPⁱ	P48735
UCD-2DPAGEⁱ	P48735

Proteomic databases

EPDⁱ	P48735
MaxQBⁱ	P48735
PaxDbⁱ	P48735
PeptideAtlasⁱ	P48735
PRIDEⁱ	P48735
ProteomicsDBⁱ	55932

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	3418
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000330062; ENSP00000331897; ENSG00000182054 [P48735-1] ENST00000540499; ENSP00000446147; ENSG00000182054 [P48735-2]
GeneIDⁱ	3418
KEGGⁱ	hsa:3418
UCSCⁱ	uc002box.4 human [P48735-1]

Organism-specific databases

CTDⁱ	3418
DisGeNETⁱ	3418
EuPathDBⁱ	HostDB:ENSG00000182054.9
GeneCardsⁱ	IDH2
HGNCⁱ	HGNC:5383 IDH2
HPAⁱ	HPA007831
MalaCardsⁱ	IDH2
MIMⁱ	137800 phenotype 147650 gene 613657 phenotype
neXtProtⁱ	NX_P48735
OpenTargetsⁱ	ENSG00000182054
Orphanetⁱ	251589 Anaplastic astrocytoma 251663 Anaplastic oligoastrocytoma 251630 Anaplastic oligodendroglioma 79315 D-2-hydroxyglutaric aciduria 296 Enchondromatosis 251601 Fibrillary astrocytoma 251604 Gemistocytic astrocytoma 163634 Maffucci syndrome 251656 Oligoastrocytoma 251627 Oligodendroglioma 251598 Protoplasmic astrocytoma
PharmGKBⁱ	PA29631
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG1526 Eukaryota COG0538 LUCA
GeneTreeⁱ	ENSGT00390000012547
HOGENOMⁱ	HOG000019858
HOVERGENⁱ	HBG006119
InParanoidⁱ	P48735
KOⁱ	K00031
OMAⁱ	FEKHYKP
OrthoDBⁱ	EOG091G06IY
PhylomeDBⁱ	P48735
TreeFamⁱ	TF300428

Enzyme and pathway databases

BioCycⁱ	MetaCyc:HS00021-MONOMER
BRENDAⁱ	1.1.1.42 2681
Reactomeⁱ	R-HSA-2151201 Transcriptional activation of mitochondrial biogenesis R-HSA-71403 Citric acid cycle (TCA cycle)
SIGNORⁱ	P48735

Miscellaneous databases

ChiTaRSⁱ	IDH2 human
GeneWikiⁱ	IDH2
GenomeRNAiⁱ	3418
Protein Ontology More...PROⁱ	PR:P48735
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000182054 Expressed in 236 organ(s), highest expression level in muscle of leg
CleanExⁱ	HS_IDH2
ExpressionAtlasⁱ	P48735 baseline and differential
Genevisibleⁱ	P48735 HS

Family and domain databases

InterProⁱ	View protein in InterPro IPR019818 IsoCit/isopropylmalate_DH_CS IPR004790 Isocitrate_DH_NADP IPR024084 IsoPropMal-DH-like_dom
PANTHERⁱ	PTHR11822 PTHR11822, 1 hit
Pfamⁱ	View protein in Pfam PF00180 Iso_dh, 1 hit
PIRSFⁱ	PIRSF000108 IDH_NADP, 1 hit
SMARTⁱ	View protein in SMART SM01329 Iso_dh, 1 hit
TIGRFAMsⁱ	TIGR00127 nadp_idh_euk, 1 hit
PROSITEⁱ	View protein in PROSITE PS00470 IDH_IMDH, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	IDHP_HUMAN
Accessionⁱ	P48735Primary (citable) accession number: P48735 Secondary accession number(s): B2R6L6, B4DFL2, Q96GT3
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
	Last sequence update:	April 3, 2002
	Last modified:	November 7, 2018
	This is version 185 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
Human chromosome 15
Human chromosome 15: entries, gene names and cross-references to MIM

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UniProtKB - P48735 (IDHP_HUMAN)

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Isocitrate dehydrogenase [NADP], mitochondrial

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GO - Biological processi

Enzyme and pathway databases

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Mitochondrion

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Sequence databases

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2D gel databases

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

Keywords - Diseaseⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ